TBG1_RAT
ID TBG1_RAT Reviewed; 451 AA.
AC P83888; Q9Z310;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tubulin gamma-1 chain;
DE AltName: Full=Gamma-1-tubulin;
DE AltName: Full=Gamma-tubulin complex component 1;
DE Short=GCP-1;
GN Name=Tubg1; Synonyms=Tubg;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10470852; DOI=10.1093/dnares/6.3.207;
RA Nakadai T., Okada N., Makino Y., Tamura T.;
RT "Structure of rat gamma-tubulin and its binding to HP33.";
RL DNA Res. 6:207-209(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. The gamma
CC chain is found at microtubule organizing centers (MTOC) such as the
CC spindle poles or the centrosome. Pericentriolar matrix component that
CC regulates alpha/beta chain minus-end nucleation, centrosome duplication
CC and spindle formation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TUBGCP2, TUBGCP3 and B9D2. Interacts with
CC CDK5RAP2; the interaction is leading to centrosomal localization of
CC TUBG1 and CDK5RAP2. Interacts with PIFO. Interacts with SAS6 and NUP62
CC at the centrosome (By similarity). Interacts with EML3 (phosphorylated
CC form) and HAUS8 (By similarity). {ECO:0000250|UniProtKB:P23258}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250|UniProtKB:P23258}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250|UniProtKB:P23258}. Note=Localizes to
CC mitotic spindle microtubules. {ECO:0000250|UniProtKB:P23258}.
CC -!- PTM: Phosphorylation at Ser-131 by BRSK1 regulates centrosome
CC duplication, possibly by mediating relocation of gamma-tubulin and its
CC associated proteins from the cytoplasm to the centrosome.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AB015946; BAA36504.1; -; mRNA.
DR EMBL; BC070957; AAH70957.1; -; mRNA.
DR RefSeq; NP_665721.1; NM_145778.2.
DR AlphaFoldDB; P83888; -.
DR SMR; P83888; -.
DR BioGRID; 251670; 3.
DR IntAct; P83888; 1.
DR STRING; 10116.ENSRNOP00000027370; -.
DR PhosphoSitePlus; P83888; -.
DR jPOST; P83888; -.
DR PaxDb; P83888; -.
DR PRIDE; P83888; -.
DR Ensembl; ENSRNOT00000027370; ENSRNOP00000027370; ENSRNOG00000020213.
DR GeneID; 252921; -.
DR KEGG; rno:252921; -.
DR UCSC; RGD:628606; rat.
DR CTD; 7283; -.
DR RGD; 628606; Tubg1.
DR eggNOG; KOG1374; Eukaryota.
DR GeneTree; ENSGT00940000156957; -.
DR HOGENOM; CLU_015718_1_0_1; -.
DR InParanoid; P83888; -.
DR OMA; EHGINKE; -.
DR OrthoDB; 687389at2759; -.
DR PhylomeDB; P83888; -.
DR TreeFam; TF300477; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:P83888; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000020213; Expressed in testis and 20 other tissues.
DR Genevisible; P83888; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISO:RGD.
DR GO; GO:0000930; C:gamma-tubulin complex; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; TAS:RGD.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000242; C:pericentriolar material; ISO:RGD.
DR GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR GO; GO:0000212; P:meiotic spindle organization; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR CDD; cd02188; gamma_tubulin; 1.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR002454; Gamma_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01164; GAMMATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..451
FT /note="Tubulin gamma-1 chain"
FT /id="PRO_0000048467"
FT BINDING 142..148
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 131
FT /note="Phosphoserine; by BRSK1"
FT /evidence="ECO:0000250|UniProtKB:P83887"
SQ SEQUENCE 451 AA; 51101 MW; A8F1068D12D0C88A CRC64;
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
IPRAVLLDLE PRVIHSILNS SYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD
VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NLIATDRLHI QNPSFSQINQ LVSTIMSAST
TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQFDKLRK REAFMEQFRK EDIFKDNFDE
MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q
